Regulation of Aquaporins by Vasopressin in the Kidney

Ikeda, Masahiro; Matsuzaki, Toshiyuki

doi:10.1016/bs.vh.2014.12.008

Cited by 26 publications

(38 citation statements)

References 125 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…AQPs, water channel proteins, are a family of transmembrane proteins. Since the isolation of AQP1 from human erythrocytes by Agre’s group in 1992 [ 21 ], thirteen aquaporins (AQP0–12) have been identified in mammals [ 22 , 23 ]. Among them, at least eight aquaporins (AQP1–4, 6–8, 11) have been found in renal epithelial cells, which are the major source of urinary EVs [ 24 ].…”

Section: Aquaporins In the Kidneymentioning

confidence: 99%

“…AQP2 was first described by Sasaki’s group in 1993 [ 30 ]; thereafter, it has become the most extensively studied AQP protein because of its regulation by vasopressin [ 23 ]. Vasopressin, secreted from the posterior pituitary in response to an increase in plasma osmolality, hypovolemia/hypotension, or both, binds to and activates the V2 vasopressin receptor on the basolateral membrane of principal cells in the kidney collecting duct ( Figure 1 ).…”

Section: Aquaporins In the Kidneymentioning

confidence: 99%

See 1 more Smart Citation

Aquaporins in Urinary Extracellular Vesicles (Exosomes)

Oshikawa¹,

Sonoda²,

Ikeda³

2016

IJMS

Self Cite

View full text Add to dashboard Cite

Since the successful characterization of urinary extracellular vesicles (uEVs) by Knepper’s group in 2004, these vesicles have been a focus of intense basic and translational research worldwide, with the aim of developing novel biomarkers and therapeutics for renal disease. Along with these studies, there is growing evidence that aquaporins (AQPs), water channel proteins, in uEVs have the potential to be diagnostically useful. In this review, we highlight current knowledge of AQPs in uEVs from their discovery to clinical application.

show abstract

Section: Aquaporins In the Kidneymentioning

confidence: 99%

Section: Aquaporins In the Kidneymentioning

confidence: 99%

Aquaporins in Urinary Extracellular Vesicles (Exosomes)

Oshikawa¹,

Sonoda²,

Ikeda³

2016

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…Les critères diagnostiques du SIADH sont repris en figure 3 13 . En terme de physiopathologie, ce phénomène pourrait s'expliquer par le fait que dans le SIADH, il y a une augmentation de l'expression des aquaporines 2 14 , et que dans le diabète insipide néphrogénique acquis provoqué par l'hypercalcémie, l'expression de ces aquaporines est diminuée 11 . Dans ce contexte, nous pouvons imaginer que les modifications induites dans le SIADH prennent le pas sur celles induites par l'hypercalcémie.…”

Section: Discussionunclassified

Study of diagnostic value of natremia in a cohort of patients with hypercalcemia

Le¹,

Couturier²,

Cogan³

et al. 2018

Rev Med Brux

View full text Add to dashboard Cite

show abstract

“…AQP1 is present in both the apical and basolateral membranes of proximal tubule cells and is involved in near-isosmolar water reabsorption (Nielsen et al, 1993). In the collecting duct system, there are three AQP isoforms (AQP2 on the luminal side, and AQP3 and AQP4 on the abluminal side) that enable urinary concentration upon vasopressin stimulation (Ikeda and Matsuzaki, 2015;Takata et al, 2008). Among these, AQP2 is a fundamental and critical molecule in vasopressin-controlled urinary concentration (Fushimi et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…One possibly important phenomenon that regulates AQP2 trafficking is its phosphorylation Ikeda and Matsuzaki, 2015). There are four serines (Sers) located near the carboxyl terminal of rat and mouse AQP2 that could be phosphorylated or dephosphorylated in response to vasopressin.…”

Section: Introductionmentioning

confidence: 99%

<b>Phosphorylation and dephosphorylation of aquaporin-2 at serine 269 and its subcellular distribution during vasopressin-induced exocytosis and subsequent endocytosis in the rat </b><b>kidney </b>

Shimizu

Sano

Kita

et al. 2017

Archives of Histology and Cytology

Self Cite

View full text Add to dashboard Cite

Summary. Aquaporin-2 (AQP2) is a water channel protein that is trafficked between intracellular vesiclesand the plasma membrane of kidney collecting duct cells upon vasopressin stimulation. Vasopressin changes the phosphorylation states of the AQP2 C-terminal serines (Sers), Ser256, Ser261, Ser264, and Ser269, in rats and mice, which is thought to play a role in controlling trafficking. Here, we focused on Ser269. We developed a specific antibody to Ser269-phosphorylated AQP2. Using immunofluorescence microscopy, we examined its localization in the rat kidney following injection of vasopressin and a vasopressin type 2 receptor-specific antagonist (OPC-31260). Ser269-phosphorylated AQP2 was almost undetectable in the water-loaded rat kidney, but was detected intracellularly soon after vasopressin injection, and then highly accumulated on the apical membrane of connecting tubule and collecting duct principal cells. In addition to the apical membrane, Ser269-phosphorylated AQP2 was also detected on the basolateral membrane of connecting tubule cells and inner medullary collecting duct principal cells. OPC-31260 injection following vasopressin stimulation caused internalization of AQP2, a pool of which was phosphorylated at Ser269. These results suggest that 1) AQP2 is phosphorylated at Ser269 intracellularly upon vasopressin stimulation and is rapidly trafficked to the plasma membrane, and 2) AQP2 can be internalized from the plasma membrane even if it remains phosphorylated at Ser269.

show abstract

Regulation of Aquaporins by Vasopressin in the Kidney

Cited by 26 publications

References 125 publications

Aquaporins in Urinary Extracellular Vesicles (Exosomes)

Aquaporins in Urinary Extracellular Vesicles (Exosomes)

Study of diagnostic value of natremia in a cohort of patients with hypercalcemia

<b>Phosphorylation and dephosphorylation of aquaporin-2 at serine 269 and its subcellular distribution during vasopressin-induced exocytosis and subsequent endocytosis in the rat </b><b>kidney </b>

Contact Info

Product

Resources

About